Single molecule fate of HIV-1 envelope reveals late-stage viral lattice incorporation
Carmen A. Buttler,
Nairi Pezeshkian,
Melissa V. Fernandez,
Jesse Aaron,
Sofya Norman,
Eric O. Freed and
Schuyler B. van Engelenburg ()
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Carmen A. Buttler: University of Denver
Nairi Pezeshkian: University of Denver
Melissa V. Fernandez: National Cancer Institute
Jesse Aaron: Howard Hughes Medical Institute
Sofya Norman: University of Denver
Eric O. Freed: National Cancer Institute
Schuyler B. van Engelenburg: University of Denver
Nature Communications, 2018, vol. 9, issue 1, 1-15
Abstract:
Abstract Human immunodeficiency virus type 1 (HIV-1) assembly occurs on the inner leaflet of the host cell plasma membrane, incorporating the essential viral envelope glycoprotein (Env) within a budding lattice of HIV-1 Gag structural proteins. The mechanism by which Env incorporates into viral particles remains poorly understood. To determine the mechanism of recruitment of Env to assembly sites, we interrogate the subviral angular distribution of Env on cell-associated virus using multicolor, three-dimensional (3D) superresolution microscopy. We demonstrate that, in a manner dependent on cell type and on the long cytoplasmic tail of Env, the distribution of Env is biased toward the necks of cell-associated particles. We postulate that this neck-biased distribution is regulated by vesicular retention and steric complementarity of Env during independent Gag lattice formation.
Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04220-w
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DOI: 10.1038/s41467-018-04220-w
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